Explore BrainMass

Explore BrainMass

    Determining Activation Energy from Rate Constant for an Enzyme-Catalyzed Reaction

    This content was COPIED from BrainMass.com - View the original, and get the already-completed solution here!

    Here is the problem I have to solve:
    If 10 g of pure carbonic anhydrase catalyzes the hydration of 0.30 g of carbon dioxide in 1 min at 37 degrees C under optimal conditions, what is the turnover number (kcat) of carbonic anhydrase (in units of min-1)?

    I have already calculated the turnover number, which is 2.0 x 107 min-1, but I'm kind of lost with two other questions.

    (b) From the answer in (a) calculate the activation energy of the enzyme catalyzed reaction (in kJ/mol)
    (c) If carbonic anhydrase provides a rate enhancement of 107, what is the activation energy for the uncatalyzed reaction?

    © BrainMass Inc. brainmass.com October 1, 2020, 7:36 pm ad1c9bdddf

    Solution Preview

    Please see attached file

    From transition-state theory, an expression can be derived that relates the magnitude of a rate constant (k) to the activation energy:

    k = (kT/h)e-G/RT

    where k is the Boltzmann constant and h is Planck's constant. In this case, G is the activation energy ...

    Solution Summary

    This solution shows step-by-step calculations to determine the activation energy of the reaction with carbonic anhydrase and also the activation energy of the uncatalyzed reaction. Brief explanations are also included.